Protein structure determination by single-wavelength anomalous diffraction 
phasing of X-ray free-electron laser data

Nass, Karol; Meinhart, Anton; Barends, Thomas R. M.; Foucar, Lutz; Gorel, Alexander; Aquila, Andrew; Botha, Sabine; Doak, R. Bruce; Koglin, Jason; Liang, Mengning; Shoeman, Robert L.; Williams, Garth; Boutet, Sebastien; Schlichting, Ilme

doi:10.1107/S2052252516002980

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Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data

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Nass, Karol
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons94313

Meinhart, Anton
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92083

Barends, Thomas R. M.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons92933

Foucar, Lutz
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons192083

Gorel, Alexander
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117990

Botha, Sabine
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons117878

Doak, R. Bruce
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95345

Shoeman, Robert L.
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

/persons/resource/persons95189

Schlichting, Ilme
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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http://journals.iucr.org/m/issues/2016/03/00/mf5014/mf5014.pdf
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http://dx.doi.org/10.1107/S2052252516002980
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Citation

Nass, K., Meinhart, A., Barends, T. R. M., Foucar, L., Gorel, A., Aquila, A., et al. (2016). Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data. IUCrJ, 3(3), 180-191. doi:10.1107/S2052252516002980.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002A-1C8F-B

Abstract

Serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs) offers unprecedented possibilities for macromolecular structure determination of systems that are prone to radiation damage. However, phasing XFEL data de novo is complicated by the inherent inaccuracy of SFX data, and only a few successful examples, mostly based on exceedingly strong anomalous or isomorphous difference signals, have been reported. Here, it is shown that SFX data from thaumatin microcrystals can be successfully phased using only the weak anomalous scattering from the endogenous S atoms. Moreover, a step-by-step investigation is presented of the particular problems of SAD phasing of SFX data, analysing data from a derivative with a strong anomalous signal as well as the weak signal from endogenous S atoms.